1PO7
HIGH RESOLUTION STRUCTURE OF E28A MUTANT BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0009056 | biological_process | catabolic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0018924 | biological_process | mandelate metabolic process |
A | 0019596 | biological_process | mandelate catabolic process |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MG A 531 |
Chain | Residue |
A | ASN117 |
A | ASN117 |
A | LEU118 |
A | LEU118 |
A | ARG120 |
A | ARG120 |
A | HOH1123 |
A | HOH1123 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 532 |
Chain | Residue |
A | ASN455 |
A | THR457 |
A | TZD530 |
A | HOH535 |
A | ASP428 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 533 |
Chain | Residue |
A | GLU37 |
A | ASP364 |
A | HOH692 |
A | HOH701 |
A | HOH1115 |
A | HOH1116 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 534 |
Chain | Residue |
A | ASP347 |
A | ALA416 |
A | HOH702 |
A | HOH713 |
A | HOH862 |
A | HOH994 |
A | HOH1014 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TZD A 530 |
Chain | Residue |
A | ASN23 |
A | PRO24 |
A | GLY25 |
A | GLU47 |
A | HIS70 |
A | ASN77 |
A | THR377 |
A | SER378 |
A | GLY401 |
A | LEU403 |
A | GLY427 |
A | ASP428 |
A | GLY429 |
A | SER430 |
A | TYR433 |
A | ASN455 |
A | THR457 |
A | TYR458 |
A | GLY459 |
A | ALA460 |
A | CA532 |
A | HOH535 |
A | HOH542 |
A | HOH628 |
Functional Information from PROSITE/UniProt
site_id | PS00187 |
Number of Residues | 20 |
Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS |
Chain | Residue | Details |
A | ILE411-SER430 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN117 | |
A | LEU118 | |
A | ARG120 | |
A | ASP428 | |
A | ASN455 | |
A | THR457 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bfd |
Chain | Residue | Details |
A | ALA28 | |
A | HIS281 | |
A | HIS70 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 220 |
Chain | Residue | Details |
A | GLY25 | electrostatic stabiliser, hydrogen bond donor |
A | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | ALA28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |